ID A0A0C2FL81_9BILA Unreviewed; 483 AA.
AC A0A0C2FL81;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Zinc metalloproteinase {ECO:0000256|PIRNR:PIRNR036365};
GN ORFNames=ANCDUO_22416 {ECO:0000313|EMBL:KIH47524.1};
OS Ancylostoma duodenale.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH47524.1, ECO:0000313|Proteomes:UP000054047};
RN [1] {ECO:0000313|EMBL:KIH47524.1, ECO:0000313|Proteomes:UP000054047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH47524.1,
RC ECO:0000313|Proteomes:UP000054047};
RA Mitreva M.;
RT "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC ECO:0000256|RuleBase:RU361183};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|PIRNR:PIRNR036365}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN767604; KIH47524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2FL81; -.
DR MEROPS; M12.310; -.
DR Proteomes; UP000054047; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR017050; Metallopeptidase_nem.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF820; ZINC METALLOPROTEINASE NAS-31; 1.
DR Pfam; PF01400; Astacin; 1.
DR PIRSF; PIRSF036365; Astacin_nematoda; 2.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS01180; CUB; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR036365};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR036365};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|PIRNR:PIRNR036365,
FT ECO:0000256|RuleBase:RU361183"
FT CHAIN 17..483
FT /note="Zinc metalloproteinase"
FT /evidence="ECO:0000256|PIRNR:PIRNR036365,
FT ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5005110934"
FT DOMAIN 104..303
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 346..464
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT ACT_SITE 201
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 483 AA; 54064 MW; C39C2291F3196687 CRC64;
MRVLLLVLLL ALCANAGFFD SKIGQKIKET LSKMKAALNG TALLKIREKF NNLKEKIKAK
LTLSPARKAI LDEILKHIKF IKRDKVQEKG DSIEEINENS NIGELLYQGD IVLTDKQAEE
IVQDIESSDS DREKRQAFRD RTYPKTLWSK GVYYYFHYNA TPDRIRVFKE EGCWSYVGRL
GGQQDLSLGD GCESVGTAAH EIGHAIGFFH TQSRHDRDNF ITFNAHNVKR DWLDQFTKQT
PATNENYGIT YDYGSIMHYG ANSATGNGRP TMVPHDPKYV ETLGSPIISF YELLMLNTHY
GCTKNCNPAT SAQCKMGGFP HPRDCSRCIC PSGYGGRLCD QKPAGCGAVY QASTQYQTFH
DEVGNKAAGQ RPREDMDFCY YWITAPQGSR IEIKIAGLSR GASVDGCQYW GVEIKTHADQ
RLTGYRFCAP EDVGTTLVST SNIVPIITYN RFFATAVDIQ YRIVSGGGNP MPQPQPNCVD
NAQ
//
